##gff-version 3
P10914	UniProtKB	Chain	1	325	.	.	.	ID=PRO_0000154545;Note=Interferon regulatory factor 1	
P10914	UniProtKB	DNA binding	5	113	.	.	.	Note=IRF tryptophan pentad repeat;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00840	
P10914	UniProtKB	Region	92	165	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P10914	UniProtKB	Compositional bias	116	143	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P10914	UniProtKB	Compositional bias	144	162	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P10914	UniProtKB	Modified residue	78	78	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22367195;Dbxref=PMID:22367195	
P10914	UniProtKB	Cross-link	275	275	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
P10914	UniProtKB	Cross-link	299	299	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)	
P10914	UniProtKB	Natural variant	8	8	.	.	.	ID=VAR_065134;Note=In GASC%3B somatic mutation%3B produces a protein with markedly reduced transcriptional activity but unaltered DNA-binding activity. M->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9679752;Dbxref=dbSNP:rs121912469,PMID:9679752	
P10914	UniProtKB	Natural variant	11	11	.	.	.	ID=VAR_065135;Note=In GASC%3B the mutation abolishes DNA binding and transactivating activities. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10395927;Dbxref=dbSNP:rs121912470,PMID:10395927	
P10914	UniProtKB	Mutagenesis	78	78	.	.	.	Note=Loss of acetylation. Partial loss of DNA-binding and transcriptional activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22367195;Dbxref=PMID:22367195	
P10914	UniProtKB	Mutagenesis	275	275	.	.	.	Note=Some loss of sumoylation. Partial inhibition of acetylation and activity. Abolishes sumoylation%2C diminished ubiquitination%2C higher resistance to degradation%2C and increased apoptotic activity%3B when associated with R-299. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17942705;Dbxref=PMID:17942705	
P10914	UniProtKB	Mutagenesis	299	299	.	.	.	Note=Large loss of sumoylation. Abolishes sumoylation%2C diminished ubiquitination%2C higher resistance to degradation%2C and increased apoptotic activity%3B when associated with R-275. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17942705;Dbxref=PMID:17942705	
P10914	UniProtKB	Sequence conflict	5	5	.	.	.	Note=R->W;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P10914	UniProtKB	Sequence conflict	34	35	.	.	.	Note=FQ->LE;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P10914	UniProtKB	Sequence conflict	220	220	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305